The Plasticity of a Translation Arrest Motif Yields Insights into Nascent Polypeptide Recognition inside the Ribosome Tunnel

Mee-Ngan Frances Yap, Harris D. Bernstein*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

Abstract

The recognition of a C-terminal motif in E. coli SecM (150FXXXXWIXXXXGIRAGP166) inside the ribosome tunnel causes translation arrest, but the mechanism of recognition is unknown. Whereas single mutations in this motif impair recognition, we demonstrate that new arrest-inducing peptides can be created through remodeling of the SecM C terminus. We found that R163 is indispensable but that flanking residues that vary in number and position play an important secondary role in translation arrest. The observation that individual SecM variants showed a distinct pattern of crosslinking to ribosomal proteins suggests that each peptide adopts a unique conformation inside the tunnel. Based on the results, we propose that translation arrest occurs when the peptide conformation specified by flanking residues moves R163 into a precise intratunnel location. Our data indicate that translation arrest results from extensive communication between SecM and the tunnel and help to explain the striking diversity of arrest-inducing peptides found throughout nature.

Original languageEnglish (US)
Pages (from-to)201-211
Number of pages11
JournalMolecular cell
Volume34
Issue number2
DOIs
StatePublished - Apr 24 2009

Keywords

  • RNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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